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Volume 2011 (2011), Article ID 308730, 9 pages
Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential
1Department of Environmental Biology, Shandong Agricultural University, Taian, Shandong 271018, China
2Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, 20521 Turku, Finland
Received 6 June 2011; Revised 5 September 2011; Accepted 7 September 2011
Academic Editor: D. M. G. Freire
Copyright © 2011 Duo-Chuan Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- D. B. Wilson, “Cellulases and biofuels,” Current Opinion in Biotechnology, vol. 20, no. 3, pp. 295–299, 2009.
- R. K. Sukumaran, V. J. Surender, R. Sindhu et al., “Lignocellulosic ethanol in India: prospects, challenges and feedstock availability,” Bioresource Technology, vol. 101, no. 13, pp. 4826–4833, 2010.
- E. Vlasenko, M. Schülein, J. Cherry, and F. Xu, “Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases,” Bioresource Technology, vol. 101, no. 7, pp. 2405–2411, 2010.
- R. Maheshwari, G. Bharadwaj, and M. K. Bhat, “Thermophilic fungi: their physiology and enzymes,” Microbiology and Molecular Biology Reviews, vol. 64, no. 3, pp. 461–488, 2000.
- M. Suto and F. Tomita, “Induction and catabolite repression mechanisms of cellulase in fungi,” Journal of Bioscience and Bioengineering, vol. 92, no. 4, pp. 305–311, 2001.
- P. G. Murray, C. M. Collins, A. Grassick, and M. G. Tuohy, “Molecular cloning, transcriptional, and expression analysis of the first cellulase gene (cbh2), encoding cellobiohydrolase II, from the moderately thermophilic fungus Talaromyces emersonii and structure prediction of the gene product,” Biochemical and Biophysical Research Communications, vol. 301, no. 2, pp. 280–286, 2003.
- A. Grassick, P. G. Murray, R. Thompson et al., “Three-dimensional structure of a thermostable native cellobiohydrolase, CBH IB, and molecular characterization of the cel7 gene from the filamentous fungus, Talaromyces emersonii,” European Journal of Biochemistry, vol. 271, no. 22, pp. 4495–4506, 2004.
- M. J. Pocas-Fonseca, I. Silva-Pereira, B. B. Rocha, and M. D. O. Azevedo, “Substrate-dependent differential expression of humicola grisea var. thermoidea cellobiohydrolase genes,” Canadian Journal of Microbiology, vol. 46, no. 8, pp. 749–752, 2000.
- C. M. Collins, P. G. Murray, S. Denman et al., “Molecular cloning and expression analysis of two distinct β-glucosidase genes, bg1 and aven1, with very different biological roles from the thermophilic, saprophytic fungus Talaromyces emersonii,” Mycological Research, vol. 111, no. 7, pp. 840–849, 2007.
- Z. Benko, E. Drahos, Z. Szengyel, T. Puranen, J. Vehmaanpera, and K. Reczey, “Thermoascus aurantiacus CBHI/Cel7A production in Trichoderma reesei on alternative carbon sources,” Applied Biochemistry and Biotechnology, vol. 137–140, no. 1–12, pp. 195–204, 2007.
- M. Ilmen, A. Saloheimo, M. L. Onnela, and M. E. Penttila, “Regulation of cellulase gene expression in the filamentous fungus Trichoderma reesei,” Applied and Environmental Microbiology, vol. 63, no. 4, pp. 1298–1306, 1997.
- T. Furukawa, Y. Shida, N. Kitagami et al., “Identification of specific binding sites for XYR1, a transcriptional activator of cellulolytic and xylanolytic genes in Trichoderma reesei,” Fungal Genetics and Biology, vol. 46, no. 8, pp. 564–574, 2009.
- S. K. Soni and R. Soni, “Regulation of cellulase synthesis in Chaetomium erraticum,” BioResources, vol. 5, no. 1, pp. 81–98, 2010.
- R. Kumar, S. Singh, and O. V. Singh, “Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives,” Journal of Industrial Microbiology and Biotechnology, vol. 35, no. 5, pp. 377–391, 2008.
- S. P. Voutilainen, T. Puranen, M. Siika-Aho, et al., “Cloning, expression, and characterization of novel thermostable family 7 cellobiohydrolases,” Biotechnology and Bioengineering, vol. 101, pp. 515–528, 2008.
- Y. L. Li, H. Li, A. N. Li, and D. C. Li, “Cloning of a gene encoding thermostable cellobiohydrolase from the thermophilic fungus Chaetomium thermophilum and its expression in Pichia pastoris,” Journal of Applied Microbiology, vol. 106, no. 6, pp. 1867–1875, 2009.
- S. Takashima, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi, “Molecular cloning and expression of the novel fungal β-glucosidase genes from Humicola grisea and Trichoderma reesei,” Journal of Biochemistry, vol. 125, no. 4, pp. 728–736, 1999.
- S. Takashima, H. Iikura, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi, “Comparison of gene structures and enzymatic properties between two endoglucanases from Humicola grisea,” Journal of Biotechnology, vol. 67, no. 2-3, pp. 85–97, 1999.
- S. Takashima, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi, “Cloning, sequencing, and expression of the cellulase genes of Humicola grisea var. thermoidea,” Journal of Biotechnology, vol. 50, no. 2-3, pp. 137–147, 1996.
- T. Moriya, M. Watanabe, N. Sumida, K. Okakura, and T. Murakami, “Cloning and overexpression of the avi2 gene encoding a major cellulase produced by Humicola insolens FERM BP-5977,” Bioscience, Biotechnology and Biochemistry, vol. 67, no. 6, pp. 1434–1437, 2003.
- P. Heinzelman, C. D. Snow, I. Wu et al., “A family of thermostable fungal cellulases created by structure-guided recombination,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 14, pp. 5610–5615, 2009.
- P. Heinzelman, C. D. Snow, M. A. Smith et al., “SCHEMA recombination of a fungal cellulase uncovers a single mutation that contributes markedly to stability,” Journal of Biological Chemistry, vol. 284, no. 39, pp. 26229–26233, 2009.
- H. Haakana, A. Miettinen-Oinonen, V. Joutsjoki, A. Mantyla, P. Suominen, and J. Vehmaanperä, “Cloning of cellulase genes from Melanocarpus albomyces and their efficient expression in Trichoderma reesei,” Enzyme and Microbial Technology, vol. 34, no. 2, pp. 159–167, 2004.
- P. Murray, N. Aro, C. Collins et al., “Expression in Trichoderma reesei and characterisation of a thermostable family 3 β-glucosidase from the moderately thermophilic fungus Talaromyces emersonii,” Protein Expression and Purification, vol. 38, no. 2, pp. 248–257, 2004.
- S. P. Voutilainen, P. G. Murray, M. G. Tuohy, and A. Koivula, “Expression of Talaromyces emersonii cellobiohydrolase Cel7A in Saccharomyces cerevisiae and rational mutagenesis to improve its thermostability and activity,” Protein Engineering, Design and Selection, vol. 23, no. 2, pp. 69–79, 2010.
- J. Hong, H. Tamaki, K. Yamamoto, and H. Kumagai, “Cloning of a gene encoding thermostable cellobiohydrolase from Thermoascus aurantiacus and its expression in yeast,” Applied Microbiology and Biotechnology, vol. 63, no. 1, pp. 42–50, 2003.
- J. Hong, H. Tamaki, K. Yamamoto, and H. Kumagai, “Cloning of a gene encoding a thermo-stable endo-β-1,4-glucanase from Thermoascus aurantiacus and its expression in yeast,” Biotechnology Letters, vol. 25, no. 8, pp. 657–661, 2003.
- J. Hong, H. Tamaki, and H. Kumagai, “Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus aurantiacus,” Applied Microbiology and Biotechnology, vol. 73, no. 6, pp. 1331–1339, 2007.
- T. Jeoh, W. Michener, M. E. Himmel, S. R. Decker, and W. S. Adney, “Implications of cellobiohydrolase glycosylation for use in biomass conversion,” Biotechnol Biofuels, vol. 1, no. 10, 2008.
- M. Meldgaard and I. Svendsen, “Different effects of N-glycosylation on the thermostability of highly homologous bacterial (1, 3-1, 4)-β-glucanases secreted from yeast,” Microbiology, vol. 140, no. 1, pp. 159–166, 1994.
- D. Mamma, D. G. Hatzinikolaou, and P. Christakopoulos, “Biochemical and catalytic properties of two intracellular β-glucosidases from the fungus Penicillium decumbens active on flavonoid glucosides,” Journal of Molecular Catalysis B, vol. 27, no. 4–6, pp. 183–190, 2004.
- S. P. Pack and Y. J. Yoo, “Protein thermostability: structure-based difference of amino acid between thermophilic and mesophilic proteins,” Journal of Biotechnology, vol. 111, no. 3, pp. 269–277, 2004.
- S. Trivedi, H. S. Gehlot, and S. R. Rao, “Protein thermostability in Archaea and Eubacteria,” Genetics and Molecular Research, vol. 5, no. 4, pp. 816–827, 2006.
- T. J. Taylor and I. I. Vaisman, “Discrimination of thermophilic and mesophilic proteins,” BMC Structural Biology, vol. 10, supplement 1, article S5, 2010.
- G. T. Beckham, Y. J. Bomble, J. F. Matthews et al., “The O-glycosylated linker from the Trichoderma reesei family 7 cellulase is a flexible, disordered protein,” Biophysical Journal, vol. 99, no. 11, pp. 3773–3781, 2010.
- H. Hashimoto, “Recent structural studies of carbohydrate-binding modules,” Cellular and Molecular Life Sciences, vol. 63, no. 24, pp. 2954–2967, 2006.
- O. Shoseyov, Z. Shani, and I. Levy, “Carbohydrate binding modules: biochemical properties and novel applications,” Microbiology and Molecular Biology Reviews, vol. 70, no. 2, pp. 283–295, 2006.
- D. J. Dagel, Y. S. Liu, L. Zhong et al., “In situ imaging of single carbohydrate-binding modules on cellulose microfibrils,” Journal of Physical Chemistry B, vol. 115, no. 4, pp. 635–641, 2011.
- A. Varrot, T. P. Frandsen, I. von Ossowski et al., “Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens,” Structure, vol. 11, no. 7, pp. 855–864, 2003.
- G. J. Davies, A. M. Brzozowski, M. Dauter, A. Varrot, and M. Schulein, “Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 Å resolution,” Biochemical Journal, vol. 348, no. 1, pp. 201–207, 2000.
- G. J. Davies, V. Ducros, R. J. Lewis, T. V. Borchert, and M. Schulein, “Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites,” Journal of Biotechnology, vol. 57, no. 1–3, pp. 91–100, 1997.
- L. F. Mackenzie, G. Sulzenbacher, C. Divne et al., “Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate,” Biochemical Journal, vol. 335, no. 2, pp. 409–416, 1998.
- G. J. Davies, G. G. Dodson, R. E. Hubbard et al., “Structure and function of endoglucanase V,” Nature, vol. 365, no. 6444, pp. 362–364, 1993.
- M. Sandgren, G. I. Berglund, A. Shaw et al., “Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A,” Journal of Molecular Biology, vol. 342, no. 5, pp. 1505–1517, 2004.
- L. Lo Leggio and S. Larsen, “The 1.62 Å structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5,” FEBS Letters, vol. 523, no. 1–3, pp. 103–108, 2002.
- M. Hirvonen and A. C. Papageorgiou, “Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms,” Journal of Molecular Biology, vol. 329, no. 3, pp. 403–410, 2003.
- T. Parkkinen, A. Koivula, J. Vehmaanpera, and J. Rouvinen, “Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding,” Protein Science, vol. 17, no. 8, pp. 1383–1394, 2008.
- S. Takashima, H. Iikura, A. Nakamura, M. Hidaka, H. Masaki, and T. Uozumi, “Isolation of the gene and characterization of the enzymatic properties of a major exoglucanase of Humicola grisea without a cellulose-binding domain,” Journal of Biochemistry, vol. 124, no. 4, pp. 717–725, 1998.
- S. Takashima, M. Ohno, M. Hidaka, A. Nakamura, H. Masaki, and T. Uozumi, “Correlation between cellulose binding and activity of cellulose-binding domain mutants of Humicola grisea cellobiohydrolase 1,” FEBS Letters, vol. 581, no. 30, pp. 5891–5896, 2007.
- L. Potterton, S. McNicholas, E. Krissinel et al., “Developments in the CCP4 molecular-graphics project,” Acta Crystallographica Section D, vol. 60, no. 12 I, pp. 2288–2294, 2004.
- M. Sandgren, P. J. Gualfetti, C. Paech et al., “The Humicola grisea Cell2A enzyme structure at 1.2 Å resolution and the impact of its free cysteine residues on thermal stability,” Protein Science, vol. 12, no. 12, pp. 2782–2793, 2003.
- J. Valjakka and J. Rouvinen, “Structure of 20K endoglucanase from Melanocarpus albomyces at 1.8 Å resolution,” Acta Crystallographica D, vol. 59, no. 4, pp. 765–768, 2003.
- Y. H. Percival Zhang, M. E. Himmel, and J. R. Mielenz, “Outlook for cellulase improvement: screening and selection strategies,” Biotechnology Advances, vol. 24, no. 5, pp. 452–481, 2006.
- N. E. Labrou, “Random mutagenesis methods for in vitro directed enzyme evolution,” Current Protein and Peptide Science, vol. 11, no. 1, pp. 91–100, 2010.
- S. P. Voutilainen, H. Boer, M. B. Linder et al., “Heterologous expression of Melanocarpus albomyces cellobiohydrolase Cel7B, and random mutagenesis to improve its thermostability,” Enzyme and Microbial Technology, vol. 41, no. 3, pp. 234–243, 2007.
- M. Sandgren, J. Stahlberg, and C. Mitchinson, “Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes,” Progress in Biophysics and Molecular Biology, vol. 89, no. 3, pp. 246–291, 2005.
- R. M. Yennamalli, A. J. Rader, J. D. Wolt, and T. Z. Sen, “Thermostability in endoglucanases is fold-specific,” BMC Structural Biology, vol. 11, Article ID 10, 2011.
- D. E. Otzen, L. Christiansen, and M. Schulein, “A comparative study of the unfolding of the endoglucanase Ce145 from Humicola insolens in denaturant and surfactant,” Protein Science, vol. 8, no. 9, pp. 1878–1887, 1999.
- S. L. Mccarter, W. S. Adney, T. B. Vinzant et al., “Exploration of cellulose surface-binding properties of Acidothermus cellulolyticus Cel5A by site-specific mutagenesis,” Applied Biochemistry and Biotechnology A, vol. 98-100, pp. 273–287, 2002.
- Y. S. Kim, H. C. Jung, and J. G. Pan, “Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants,” Applied and Environmental Microbiology, vol. 66, no. 2, pp. 788–793, 2000.
- J. Ni, M. Takehara, and H. Watanabe, “Identification of activity related amino acid mutations of a GH9 termite cellulase,” Bioresource Technology, vol. 101, no. 16, pp. 6438–6443, 2010.
- S. P. Voutilainen, H. Boer, M. Alapuranen, J. Janis, J. Vehmaanpera, and A. Koivula, “Improving the thermostability and activity of Melanocarpus albomyces cellobiohydrolase Cel7B,” Applied Microbiology and Biotechnology, vol. 83, no. 2, pp. 261–272, 2009.
- M. C. Limon, E. Margolles-Clark, T. Benitez, and M. Penttila, “Addition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum,” FEMS Microbiology Letters, vol. 198, no. 1, pp. 57–63, 2001.
- N. Szijarto, M. Siika-aho, M. Tenkanen et al., “Hydrolysis of amorphous and crystalline cellulose by heterologously produced cellulases of Melanocarpus albomyces,” Journal of Biotechnology, vol. 136, no. 3-4, pp. 140–147, 2008.
- F. A. Shaikh and S. G. Withers, “Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis,” Biochemistry and Cell Biology, vol. 86, no. 2, pp. 169–177, 2008.
- S. Fort, V. Boyer, L. Greffe et al., “Highly efficient synthesis of β-oligo- and -polysaccharides using a mutant cellulase,” Journal of the American Chemical Society, vol. 122, no. 23, pp. 5429–5437, 2000.
- S. Blanchard, S. Armand, P. Couthino et al., “Unexpected regioselectivity of Humicola insolens Cel7B glycosynthase mutants,” Carbohydrate Research, vol. 342, no. 5, pp. 710–716, 2007.